Abstract
Partial characterization of the crude proteolytic extracts of five Asclepiadaceae species namely Araujia hortorum Fourn., Asclepias curassavica L., Funastrum clausum (Jacq.) Schlechter, Morrenia brachystephana Griseb. and Morrenia odorata (Hook. et Arn.) Lindley, and a comparison of these results and those from other Asclepiadaceae species are reported. Additionally, the crude extract from M. brachystephana was submitted to further purification and characterization. The crude enzyme showed high proteolytic activity when assayed on casein in the presence of 12 mM cysteine but was strongly inhibited by very low concentrations of sodium iodoacetate (0.01 mM) and mercuric chloride (0.1 mM) suggesting that the enzyme belongs to the cysteinyl-proteases type. Fractioned acetone precipitation followed by cation exchange chromatography allowed the separation of two basic ( pI > 9.3) proteolytically active fractions, both homogeneous by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and with similar molecular masses (25.5 and 26 kDa).Copyright © 1998 John Wiley & Sons, Ltd.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
